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Conserved domains on  [gi|2320403068|ref|WP_263756121|]
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formylglycine-generating enzyme family protein, partial [Leclercia adecarboxylata]

Protein Classification

formylglycine-generating enzyme family protein( domain architecture ID 11441389)

formylglycine-generating enzyme family protein similar to human sulfatase-modifying factor 1 (SUMF1), which oxidizes a cysteine residue in the substrate sulfatase, to an active site 3-oxoalanine residue, also called C(alpha)-formylglycine

CATH:  3.90.1580.10
PubMed:  30824597|27862795|18625336
SCOP:  4000450

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
 2-87 2.44e-14

Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440874 [Multi-domain]  Cd Length: 238  Bit Score: 66.18  E-value: 2.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320403068   2 GVFSPLPGNLYPPNPLGIYDMAGNGWEWIKDWYDPdYYKYSPVKNPQGPEKpmfkdsrgNYTRVIRSQDYSGPRRGATI- 80
Cdd:COG1262   146 GRGSTAPVGSFPPNPFGLYDMAGNVWEWTADWYDP-PYPGAPADGPVGPEN--------GGQRVLRGGSWATPPDHLRSa 216


                  ....*..
gi 2320403068  81 FRFFSDP 87
Cdd:COG1262   217 YRNFFPP 223
 
Name Accession Description Interval E-value
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
 2-87 2.44e-14

Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440874 [Multi-domain]  Cd Length: 238  Bit Score: 66.18  E-value: 2.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320403068   2 GVFSPLPGNLYPPNPLGIYDMAGNGWEWIKDWYDPdYYKYSPVKNPQGPEKpmfkdsrgNYTRVIRSQDYSGPRRGATI- 80
Cdd:COG1262   146 GRGSTAPVGSFPPNPFGLYDMAGNVWEWTADWYDP-PYPGAPADGPVGPEN--------GGQRVLRGGSWATPPDHLRSa 216


                  ....*..
gi 2320403068  81 FRFFSDP 87
Cdd:COG1262   217 YRNFFPP 223
FGE-sulfatase pfam03781
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
 3-61 2.40e-10

Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.


Pssm-ID: 397722 [Multi-domain]  Cd Length: 259  Bit Score: 55.58  E-value: 2.40e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2320403068   3 VFSPLPGNLYPPNPLGIYDMAGNGWEWIKDWYDPDYYKYSPVKNPQGPEKPMFKDSRGN 61
Cdd:pfam03781 166 NGRTSPVGSFPPNALGLYDMAGNVWEWTSDWYKPHYSFAPYDELSRDNFGGGYRVVRGG 224
 
Name Accession Description Interval E-value
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
 2-87 2.44e-14

Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440874 [Multi-domain]  Cd Length: 238  Bit Score: 66.18  E-value: 2.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320403068   2 GVFSPLPGNLYPPNPLGIYDMAGNGWEWIKDWYDPdYYKYSPVKNPQGPEKpmfkdsrgNYTRVIRSQDYSGPRRGATI- 80
Cdd:COG1262   146 GRGSTAPVGSFPPNPFGLYDMAGNVWEWTADWYDP-PYPGAPADGPVGPEN--------GGQRVLRGGSWATPPDHLRSa 216


                  ....*..
gi 2320403068  81 FRFFSDP 87
Cdd:COG1262   217 YRNFFPP 223
FGE-sulfatase pfam03781
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
 3-61 2.40e-10

Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.


Pssm-ID: 397722 [Multi-domain]  Cd Length: 259  Bit Score: 55.58  E-value: 2.40e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2320403068   3 VFSPLPGNLYPPNPLGIYDMAGNGWEWIKDWYDPDYYKYSPVKNPQGPEKPMFKDSRGN 61
Cdd:pfam03781 166 NGRTSPVGSFPPNALGLYDMAGNVWEWTSDWYKPHYSFAPYDELSRDNFGGGYRVVRGG 224
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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